ID A0A1G2UJP7_9BACT Unreviewed; 471 AA.
AC A0A1G2UJP7;
DT 15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT 15-FEB-2017, sequence version 1.
DT 27-MAR-2024, entry version 19.
DE RecName: Full=methionine--tRNA ligase {ECO:0000256|ARBA:ARBA00012838};
DE EC=6.1.1.10 {ECO:0000256|ARBA:ARBA00012838};
GN ORFNames=A3H60_00460 {ECO:0000313|EMBL:OHB09656.1};
OS Candidatus Zambryskibacteria bacterium RIFCSPLOWO2_02_FULL_44_12b.
OC Bacteria; Candidatus Zambryskibacteria.
OX NCBI_TaxID=1802772 {ECO:0000313|EMBL:OHB09656.1, ECO:0000313|Proteomes:UP000177202};
RN [1] {ECO:0000313|EMBL:OHB09656.1, ECO:0000313|Proteomes:UP000177202}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=27774985; DOI=10.1038/ncomms13219;
RA Anantharaman K., Brown C.T., Hug L.A., Sharon I., Castelle C.J.,
RA Probst A.J., Thomas B.C., Singh A., Wilkins M.J., Karaoz U., Brodie E.L.,
RA Williams K.H., Hubbard S.S., Banfield J.F.;
RT "Thousands of microbial genomes shed light on interconnected biogeochemical
RT processes in an aquifer system.";
RL Nat. Commun. 7:13219-13219(2016).
CC -!- SIMILARITY: Belongs to the class-I aminoacyl-tRNA synthetase family.
CC {ECO:0000256|RuleBase:RU363039}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:OHB09656.1}.
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DR EMBL; MHWP01000029; OHB09656.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1G2UJP7; -.
DR STRING; 1802772.A3H60_00460; -.
DR Proteomes; UP000177202; Unassembled WGS sequence.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004825; F:methionine-tRNA ligase activity; IEA:UniProtKB-EC.
DR GO; GO:0006431; P:methionyl-tRNA aminoacylation; IEA:InterPro.
DR Gene3D; 2.170.220.10; -; 1.
DR Gene3D; 3.40.50.620; HUPs; 1.
DR InterPro; IPR023457; Met-tRNA_synth_2.
DR InterPro; IPR015413; Methionyl/Leucyl_tRNA_Synth.
DR InterPro; IPR033911; MetRS_core.
DR InterPro; IPR014729; Rossmann-like_a/b/a_fold.
DR InterPro; IPR009080; tRNAsynth_Ia_anticodon-bd.
DR PANTHER; PTHR43326:SF1; METHIONINE--TRNA LIGASE, MITOCHONDRIAL; 1.
DR PANTHER; PTHR43326; METHIONYL-TRNA SYNTHETASE; 1.
DR Pfam; PF09334; tRNA-synt_1g; 1.
DR PRINTS; PR01041; TRNASYNTHMET.
DR SUPFAM; SSF47323; Anticodon-binding domain of a subclass of class I aminoacyl-tRNA synthetases; 1.
DR SUPFAM; SSF52374; Nucleotidylyl transferase; 1.
PE 3: Inferred from homology;
KW Aminoacyl-tRNA synthetase {ECO:0000256|ARBA:ARBA00023146,
KW ECO:0000256|RuleBase:RU363039};
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|RuleBase:RU363039};
KW Ligase {ECO:0000256|ARBA:ARBA00022598, ECO:0000256|RuleBase:RU363039};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|RuleBase:RU363039};
KW Protein biosynthesis {ECO:0000256|ARBA:ARBA00022917,
KW ECO:0000256|RuleBase:RU363039}.
FT DOMAIN 139..364
FT /note="Methionyl/Leucyl tRNA synthetase"
FT /evidence="ECO:0000259|Pfam:PF09334"
SQ SEQUENCE 471 AA; 54569 MW; AAD04209D96785FF CRC64;
MPHNKSFYIT TTLPYVNAEP HIGFAMEIIH ADIVARAKEL QDYEVFFNTG TDEHGMKIYQ
KAFDFDKSPQ EYVDAAVVKF KDLKKLLNLS SDIHFVRTTD PHHIFAAQEF WKQCDANGYI
YKKKYKAKYC VGCELERTDS EIENGKCFIH QDKDLEIIEE ENYFFKFSAF QKPLLKFYKK
NPDFVIPSSR FNEVIRFVES GLEDFSISRL KSKMSWGVTV PGDDRHVMYV WFDALVNYIS
TIGWPDNKDE FDKWWPVVQF AGKDQVRQQA AMWQAMLMSV GLVPSQQIVI HGFVNFGGQK
MSKSLGNVIS PNKVLSRFNL DTLRYFVTRE FNQFEDTDIS WEKFLESYNA NLANGLGNLV
ARIMKLAETY LSKPVTVQHS VLNKEVVDFL DKFEIQKAAN HIWEQIGELD AEIQESKPWE
SKDKEIIGGL VVKLAHIGYS LTPFIPQTSE KILKAIKENK MPETLFPRKD A
//
